Heat Shock Factor Protein 1 (HSF1) antibody

Details for Product No. ABIN361703
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Antigen
Synonyms hsf1, Hsf, xhsf1, AA960185, HSTF1, HSF1, HSF, HSF1c, hsf1a, hsf1b, zHSF1a, zHSF1b, hstf1
Reactivity
Human, Mouse (Murine), Cow (Bovine), Guinea Pig, Hamster, Monkey, Rabbit
(259), (212), (87), (56), (40), (39), (39), (39), (24), (24), (2), (2), (1), (1), (1)
Host
Rat
(201), (111), (22), (1)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(11), (11), (11), (7), (7), (5), (5), (5), (5), (5), (5), (5), (5), (5), (5), (5), (4), (4), (4), (4), (4), (4), (4), (4), (3), (2), (2)
Application
Western Blotting (WB), Immunoprecipitation (IP), Immunocytochemistry (ICC), ELISA, Gel Shift (GS)
(269), (179), (114), (105), (99), (74), (40), (40), (38), (1), (1)
Pubmed 12 references available
Quantity 25 μg
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Catalog No. ABIN361703
156.20 $
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Immunogen Purified recombinant HSF1 protein
Clone 10H8
Isotype IgG1
Specificity Detects an approx. 85 kDa protein in unstressed cell lysates, and an approx. 95 kDa protein in heat shocked cell lysates, corresponding to the molecular mass of inactive and active forms of HSF1 on SDS PAGE immunoblots.
Sensitivity 1 µg/mL of SMC-118 was sufficient for detection of HSF1 in 20 µg of heat shocked HeLa cell lysate by ECL immunoblot analysis using Goat anti-rat IgG:HRP as the secondary antibody
Purification Protein G Purified
Alternative Name HSF1
Background Synonyms:
HSTF1
HSF1, or heat shock factor 1, belongs to a family of Heat Shock transcription factors that activate the transcription of genes encoding products required for protein folding, processing, targeting, degradation, and function. The up-regulation of HSP (heat shock proteins) expression by stressors is achieved at the level of transcription through a heat shock element (HSE) and a transcription factor (HSF).Most HSFs have highly conserved amino acid sequences. On all HSFs there is a DNA binding domain at the N-terminus. Hydrophobic repeats located adjacent to this binding domain are essential for the formation of active trimers. Towards the C-terminal region another short hydrophobic repeat exists, and is thought to be necessary for suppression of trimerization.There are two main heat shock factors, 1 and 2. MouseHSF1 exists as two isoforms, however in higher eukaryotes HSF1 is found in a diffuse cytoplasmic and nuclear distribution in un-stressed cells. Once exposed to a multitude of stressors, it localizes to discrete nuclear granules within seconds. As it recovers from stress, HSF1 dissipates from these granules to a diffuse nuceloplasmic distribution. HSF2 on the other hand is similar to mouse HSF1, as it exists as two isoforms, the alpha form being more transcriptionally active than the smaller beta form. Various experiments have suggested that HFS2 may have roles in differentiation and development.
Gene ID 3297
NCBI Accession NP_005517
UniProt Q00613
Research Area Chromatin and Nuclear Signaling, Transcription Factors, Heat Shock Proteins, Neurology
Application Notes Recommended Dilution: 1 µg/mL was sufficient for detection of HSF1 by ECL imm µnoblot in 20 µg of HeLa lysate.
Restrictions For Research Use only
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
anti-Heat Shock Factor Protein 1 (HSF1) antibody HSF1 (10H8), HeLa cells mitosis
Background publications Goodson, Park-Sarge, Sarge: "Tissue-dependent expression of heat shock factor 2 isoforms with distinct transcriptional activities." in: Molecular and cellular biology, Vol. 15, Issue 10, pp. 5288-93, 1995 (PubMed).

Fiorenza, Farkas, Dissing et al.: "Complex expression of murine heat shock transcription factors." in: Nucleic acids research, Vol. 23, Issue 3, pp. 467-74, 1995 (PubMed).

Murphy, Gorzowski, Sarge et al.: "Characterization of constitutive HSF2 DNA-binding activity in mouse embryonal carcinoma cells." in: Molecular and cellular biology, Vol. 14, Issue 8, pp. 5309-17, 1994 (PubMed).

Sarge, Park-Sarge, Kirby et al.: "Expression of heat shock factor 2 in mouse testis: potential role as a regulator of heat-shock protein gene expression during spermatogenesis." in: Biology of reproduction, Vol. 50, Issue 6, pp. 1334-43, 1994 (PubMed).

Rallu, Loones, Lallemand et al.: "Function and regulation of heat shock factor 2 during mouse embryogenesis." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, Issue 6, pp. 2392-7, 1997 (PubMed).

Cotto, Fox, Morimoto: "HSF1 granules: a novel stress-induced nuclear compartment of human cells." in: Journal of cell science, Vol. 110 ( Pt 23), pp. 2925-34, 1998 (PubMed).

McMillan, Xiao, Shao et al.: "Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis." in: The Journal of biological chemistry, Vol. 273, Issue 13, pp. 7523-8, 1998 (PubMed).

Morimoto: "Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators." in: Genes & development, Vol. 12, Issue 24, pp. 3788-96, 1999 (PubMed).

Jolly, Usson, Morimoto: "Rapid and reversible relocalization of heat shock factor 1 within seconds to nuclear stress granules." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, Issue 12, pp. 6769-74, 1999 (PubMed).

Morano, Thiele: "Heat shock factor function and regulation in response to cellular stress, growth, and differentiation signals." in: Gene expression, Vol. 7, Issue 4-6, pp. 271-82, 1999 (PubMed).

General Tanaka, Namba, Arai et al.: "Genetic evidence for a protective role for heat shock factor 1 and heat shock protein 70 against colitis." in: The Journal of biological chemistry, Vol. 282, Issue 32, pp. 23240-52, 2007 (PubMed).

Monechi, Fiumalbi, De Monte et al.: "[Investigation on health status of silica exposed workers in "cotto Fiorentino" companies]" in: Giornale italiano di medicina del lavoro ed ergonomia, Vol. 29, Issue 3 Suppl, pp. 736-7, 2008 (PubMed).

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